Conformational analysis and hemolytic activity of immunoglobulin G fragment 285-292 and its analogs

Theoretical conformational analysis was carried out for the 285-292 fragment of human immunoglobulin G (His-Asn-Ala-Lys-Thr-Lys-Pro-Arg) and its analogues containing Arg, Glu, Gly, Lys, or Trp residue instead of the His residue in position 1. Spectropolarimetic investigation of these peptides showed...

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Bibliographic Details
Published in:	Bioorganicheskaia khimiia Vol. 20; no. 6; p. 617
Main Authors:	Kolobov, A A, Kolodkin, N I, Olennikova, L V, Ishchenko, A M, Kaurov, O A
Format:	Journal Article
Language:	Russian
Published:	Russia (Federation) 01-06-1994
Subjects:	Complement C1q - immunology Erythrocytes - immunology Hemolysis Humans Immunoglobulin Fragments - chemistry Immunoglobulin Fragments - immunology Immunoglobulin G - chemistry Immunoglobulin G - immunology Protein Binding Protein Conformation Spectrum Analysis
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Summary:	Theoretical conformational analysis was carried out for the 285-292 fragment of human immunoglobulin G (His-Asn-Ala-Lys-Thr-Lys-Pro-Arg) and its analogues containing Arg, Glu, Gly, Lys, or Trp residue instead of the His residue in position 1. Spectropolarimetic investigation of these peptides showed the analogues to have different activities in the C1q-mediated erythrocytes hemolysis assay. Comparison of the low-energy structures sets of the compounds tested allowed to suggest a model of the "biological active" conformation for the peptide molecule in the course of the C1q complement component binding.
ISSN:	0132-3423